Pharmacokinetics of Synthetic Human Parathyroid Hormone 1-34 in man Measured by Cytochemical Bioassay and Radioimmunoassay

1985 ◽  
Vol 68 (2) ◽  
pp. 171-177 ◽  
Author(s):  
G. N. Kent ◽  
N. Loveridge ◽  
J. Reeve ◽  
Joan M. Zanelli
Keyword(s):  
Parathyroid Hormone ◽  
Intravenous Injection ◽  
Time Course ◽  
Biologically Active ◽  
Biological Degradation ◽  
Human Parathyroid Hormone ◽  
Subcutaneous Injections ◽  
Cytochemical Bioassay ◽  
Specific Radioimmunoassay ◽  
Transit Times

1. Synthetic human parathyroid hormone (hPTH) 1-34 was given by intravenous injection to two healthy men. The time course of its appearance in and disappearance from the plasma was monitored both by cytochemical bioassay and by a specific radioimmunoassay (RIA) system. 2. Immunoreactive N-region parathyroid hormone (iPTH) reached peak concentrations in plasma at 2 min after injection, whereas peak concentrations of biologically active parathyroid hormone (bioPTH) were delayed until 4-6 min. Bioassayable PTH-like activity then disappeared from the plasma (mean transit times 5.8 and 8.6 min), approximately twice as fast as immuno-reactivity. 3. After separate subcutaneous administrations, a calculated 22-37% of administered hPTH 1-34 was subsequently detected in the plasma, by both assay systems. 4. It was not possible to explain fully the non-parallel appearances of bio- and immuno-reactivities in the plasma after intravenous injection nor the non-parallel disappearances after both intravenous and subcutaneous injections on the basis of the present data. It seems likely, however, that in the process of biological degradation the immunoreactive locus is inactivated by a different reaction from that which destroys bioactivity. 5. To investigate these activity dissociations further will require the application of microfractionation procedures in conjunction with both types of assay system.

Analysis of immunoreactive and biologically active human parathyroid hormone-peptides by high-performance-liquid-chromatography

1984 ◽  
Vol 107 (1) ◽  
pp. 60-69 ◽  
Author(s):  
T. Schettler ◽  
B. Aufm' Kolk ◽  
M.J. Atkinson ◽  
H. Radeke ◽  
C. Enters ◽  
...  
Keyword(s):  
Parathyroid Hormone ◽  
Parathyroid Adenoma ◽  
High Performance ◽  
Biologically Active ◽  
Peptide Sequence ◽  
Human Parathyroid Hormone ◽  
Healthy Individuals ◽  
In Vitro Bioassay

Abstract. A combination of high-performance-liquidchromatography (HPLC), sensitive radioimmunoassays and a homologous in vitro bioassay was used to characterise human parathyroid hormone (hPTH)-peptides in human parathyroid adenoma and plasma. Chromatography of several synthetic hPTH-peptides allows the calibration of the HPLC column. On the basis of sequence hydrophobicity the elution position of peptides can be predicted. A model for the determination of the minimal peptide sequence of each peptide has been developed which based on immunological and physicochemical properties allows the characterisation of unknown hPTH-peptides. Using this technique the heterogeneity of circulating hPTH-peptides in human plasma has been examined. Plasma extracts from healthy individuals, osteoporotic, hyperparathyroid and pseudohyperparathyroid patients were investigated. A uniform pattern in the heterogeneity of hPTH-peptides was detected. Using parathyroid adenoma as reference disease specific changes were characterised.

scholarly journals Preparation of biologically active tritium-labelled 1-34 human parathyroid hormone

FEBS Letters ◽  
1977 ◽  
Vol 78 (2) ◽  
pp. 237-243 ◽  
Author(s):  
D. Chansel ◽  
J. Sraer ◽  
J.L. Morgat ◽  
R.D. Hesch ◽  
R. Ardaillou
Keyword(s):  
Parathyroid Hormone ◽  
Biologically Active ◽  
Human Parathyroid Hormone

Endogenous Biologically Active Human Parathyroid Hormone: Measurement by a Guanyl Nucleotide-Amplified Renal Adenylate Cyclase Assay*

1981 ◽  
Vol 52 (5) ◽  
pp. 840-846 ◽  
Author(s):  
ROBERT A. NISSENSON ◽  
STEPHEN R. ABBOTT ◽  
ANNE P. TEITELBAUM ◽  
ORLO H. CLARK ◽  
CLAUDE D. ARNAUD
Keyword(s):  
Parathyroid Hormone ◽  
Adenylate Cyclase ◽  
Biologically Active ◽  
Human Parathyroid Hormone

Skeletal Changes in Rats Given Daily Subcutaneous Injections of Recombinant Human Parathyroid Hormone (1-34) for 2 Years and Relevance to Human Safety

2002 ◽  
Vol 30 (3) ◽  
pp. 312-321 ◽  
Author(s):  
John L. Vahle ◽  
Masahiko Sato ◽  
Gerald G. Long ◽  
Jamie K. Young ◽  
Paul C. Francis ◽  
...  
Keyword(s):  
Parathyroid Hormone ◽  
Human Parathyroid Hormone ◽  
Subcutaneous Injections ◽  
Human Safety ◽  
Skeletal Changes

scholarly journals Extraction and purification of recombinant intact human Parathyroid Hormone (hPTH) from bacterial cell

2017 ◽  
Vol 3 (2) ◽  
pp. 1 ◽  
Author(s):  
Adnan E. Al-badran ◽  
Rafeef Amer Abdul-jabbar
Keyword(s):  
Biological Activity ◽  
Parathyroid Hormone ◽  
Bacterial Cell ◽  
Biologically Active ◽  
Human Parathyroid Hormone ◽  
Hormone Production ◽  
Rp Hplc ◽  
Bioactivity Assay ◽  
Significant Difference ◽  
Mcf 7

Objective: The intact human Parathyroid hormone (hPTH) is one of the biopharmaceutical drug produced by biotechnology, this hormone can be provided in a good amount using simple batch culture, and therefore the main purpose of this study was the production of purified bioactive intact hPTH.Methods: A cloning BL21(DE3) strain (which already cloned in our Lab. by synthetic human Parathyroid hormone (shPTH) gene) was grown in LB medium and the cloning gene expression was induced by addition of IPTG to the medium. The recombinant fused protein was purified from the bacterial cell lysate by affinity chromatography and underwent proteolysis by Enterokinase enzyme to obtain the target hPTH, and it's further purified by DEAE and SP Sepharose ion exchange chromatography. RP-HPLC analysis and biological activity on the MCF-7 breast cancer cells were done for both the standard and produced hPTH. Furthermore, the haemolysis ability of the latter was tested on the human RBC.Results: 225ng/ml of hPTH was produced after SP chromatography which detected by specific PTH ELISA kit, standard and produced hPTH showed the same peaks in the same retention time when analyzed by HPLC. The produced hPTH haemolysis assay showed the ability of the produced hPTH to partially haemolyze the RBC in a concentration above 200µg/ml. The bioactivity assay for the produced and standard rhPTH demonstrated that both compounds had a biological activity on the MCF-7 cells with IC50 of about 84.4 and 75.7 µg/ml for standard and produced hPTH respectively, and no significant difference was detected between them.Conclusions: Via suitable purification processes, the biologically active hPTH with structure similar to the standard ones as detected by RP-HPLC and bioactivity assay, can be obtained by using already cloned isolate with shPTH gene for hormone production. The hormone showed haemolysis effect on the RBC similar to the normal secreted hPTH.

Sign in / Sign up

Export Citation Format

Share Document